Tag | Content |
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CPLM ID | CPLM-002948 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Glutamate--cysteine ligase |
Protein Synonyms/Alias | Gamma-ECS; GCS; Gamma-glutamylcysteine synthetase |
Gene Name | gshA |
Gene Synonyms/Alias | gsh-I; b2688; JW2663 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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220 | PTSLPFEKTECGMYY | acetylation | [1] | 276 | TPSEEYAKIGIEKDG | acetylation | [1] | 281 | YAKIGIEKDGKRLQI | acetylation | [1] | 465 | TGIGGTGKAFAEAYR | acetylation | [1] | 516 | PFAVWLEKHA***** | acetylation | [1] |
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Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | |
Sequence Annotation | |
Keyword | 3D-structure; ATP-binding; Complete proteome; Glutathione biosynthesis; Ligase; Nucleotide-binding; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 518 AA |
Protein Sequence | MIPDVSQALA WLEKHPQALK GIQRGLERET LRVNADGTLA TTGHPEALGS ALTHKWITTD 60 FAEALLEFIT PVDGDIEHML TFMRDLHRYT ARNMGDERMW PLSMPCYIAE GQDIELAQYG 120 TSNTGRFKTL YREGLKNRYG ALMQTISGVH YNFSLPMAFW QAKCGDISGA DAKEKISAGY 180 FRVIRNYYRF GWVIPYLFGA SPAICSSFLQ GKPTSLPFEK TECGMYYLPY ATSLRLSDLG 240 YTNKSQSNLG ITFNDLYEYV AGLKQAIKTP SEEYAKIGIE KDGKRLQINS NVLQIENELY 300 APIRPKRVTR SGESPSDALL RGGIEYIEVR SLDINPFSPI GVDEQQVRFL DLFMVWCALA 360 DAPEMSSSEL ACTRVNWNRV ILEGRKPGLT LGIGCETAQF PLPQVGKDLF RDLKRVAQTL 420 DSINGGEAYQ KVCDELVACF DNPDLTFSAR ILRSMIDTGI GGTGKAFAEA YRNLLREEPL 480 EILREEDFVA EREASERRQQ EMEAADTEPF AVWLEKHA 518 |
Gene Ontology | GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0004357; F:glutamate-cysteine ligase activity; IDA:EcoCyc. GO:0046872; F:metal ion binding; IDA:EcoCyc. GO:0071243; P:cellular response to arsenic-containing substance; IMP:EcoCyc. GO:0071288; P:cellular response to mercury ion; IMP:EcoCyc. GO:0006750; P:glutathione biosynthetic process; IMP:EcoCyc. GO:0006972; P:hyperosmotic response; IMP:EcoCyc. |
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PROSITE | |
PRINTS | |